This laboratory is interested in the relationship among protein sequence, structure and the mechanisms of protein folding and enzymic reactions. (i) Secondary Structure of Amyloid Proteins. [unreadable] g-factor analysis of the CD spectra of amyloid proteins and polypeptides indicate the presence of two types of structure. Amyloid forms of ovalbumin, apomyoglobin, transthyretin and Ure2p contain 35-55% of beta sheet, whose CD spectrum is like that found in most globular proteins. The more intense spectra of beta-2-microglobulin, insulin, Abeta(1-40) peptide and various homopolypetides, in amyloid films are consistent with the presence of 50-80% of beta helix like structure. The latter result is compatible with a protofibril which contains a structural unit of approximately 45 residues in a beta helix like structure. I am investigating the behavior of peptides known to form anti-parallel sheets as a way to validate these assignments.[unreadable]